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1st4

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1st4, resolution 2.02Å ()
Ligands: ,
Gene: DCPS (Homo sapiens)
Domains: DcpS
Related: 1st0
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of DcpS bound to m7GpppA

Publication Abstract from PubMed

Complete removal of residual N-7 guanine cap from degraded messenger RNA is necessary to prevent accumulation of intermediates that might interfere with RNA processing, export, and translation. The human scavenger decapping enzyme, DcpS, catalyzes residual cap hydrolysis following mRNA degradation, releasing N-7 methyl guanosine monophosphate and 5'-diphosphate terminated cap or mRNA products. DcpS structures bound to m(7)GpppG or m(7)GpppA reveal an asymmetric DcpS dimer that simultaneously creates an open nonproductive DcpS-cap complex and a closed productive DcpS-cap complex that alternate via 30 A domain movements. Structural and biochemical analysis suggests an autoregulatory mechanism whereby premature decapping mRNA is prevented by blocking the conformational changes that are required to form a closed productive active site capable of cap hydrolysis.

Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity., Gu M, Fabrega C, Liu SW, Liu H, Kiledjian M, Lima CD, Mol Cell. 2004 Apr 9;14(1):67-80. PMID:15068804

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1ST4 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Gu M, Fabrega C, Liu SW, Liu H, Kiledjian M, Lima CD. Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity. Mol Cell. 2004 Apr 9;14(1):67-80. PMID:15068804

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